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Protein

FYVE, RhoGEF and PH domain-containing protein 1

Gene

FGD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri730 – 79061FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. guanyl-nucleotide exchange factor activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. Rho guanyl-nucleotide exchange factor activity Source: InterPro
  4. small GTPase binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. apoptotic signaling pathway Source: Reactome
  3. cytoskeleton organization Source: UniProtKB
  4. filopodium assembly Source: UniProtKB
  5. multicellular organismal development Source: ProtInc
  6. neurotrophin TRK receptor signaling pathway Source: Reactome
  7. organ morphogenesis Source: ProtInc
  8. positive regulation of apoptotic process Source: Reactome
  9. positive regulation of GTPase activity Source: GOC
  10. regulation of cell shape Source: UniProtKB
  11. regulation of GTPase activity Source: UniProtKB
  12. regulation of small GTPase mediated signal transduction Source: Reactome
  13. signal transduction Source: ProtInc
  14. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
FYVE, RhoGEF and PH domain-containing protein 1
Alternative name(s):
Faciogenital dysplasia 1 protein
Rho/Rac guanine nucleotide exchange factor FGD1
Short name:
Rho/Rac GEF
Zinc finger FYVE domain-containing protein 3
Gene namesi
Name:FGD1
Synonyms:FGDY, ZFYVE3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3663. FGD1.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Cell projectionlamellipodium By similarity
  3. Cell projectionruffle By similarity
  4. Cytoplasmcytoskeleton By similarity

  5. Note: Associated with membrane ruffles and lamellipodia.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. Golgi apparatus Source: UniProtKB
  5. lamellipodium Source: UniProtKB
  6. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Aarskog-Scott syndrome (AAS)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare multisystemic disorder characterized by disproportionately short stature, and by facial, skeletal and urogenital anomalies. Some patients manifest mental retardation, attention deficit disorder and hyperactivity.

See also OMIM:305400
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti205 – 2051S → I in AAS. 1 Publication
VAR_019268
Natural varianti380 – 3801E → A in AAS. 1 Publication
VAR_019270
Natural varianti443 – 4431R → H in AAS. 1 Publication
VAR_019271
Natural varianti522 – 5221R → H in AAS. 1 Publication
VAR_015236
Natural varianti610 – 6101R → Q in AAS. 1 Publication
Corresponds to variant rs28935497 [ dbSNP | Ensembl ].
VAR_015237

Defects in FGD1 are found in a patient with non-syndromal X-linked mental retardation.

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi305400. phenotype.
Orphaneti915. Aarskog-Scott syndrome.
PharmGKBiPA28102.

Polymorphism and mutation databases

BioMutaiFGD1.
DMDMi28202247.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 961961FYVE, RhoGEF and PH domain-containing protein 1PRO_0000080940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphoserine1 Publication
Modified residuei205 – 2051Phosphoserine1 Publication
Modified residuei711 – 7111Phosphothreonine1 Publication
Modified residuei715 – 7151Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP98174.
PaxDbiP98174.
PRIDEiP98174.

PTM databases

PhosphoSiteiP98174.

Expressioni

Tissue specificityi

Expressed in fetal heart, brain, lung, kidney and placenta. Less expressed in liver; adult heart, brain, lung, pancreas and skeletal muscle.

Gene expression databases

BgeeiP98174.
CleanExiHS_FGD1.
ExpressionAtlasiP98174. baseline and differential.
GenevestigatoriP98174.

Organism-specific databases

HPAiHPA000911.

Interactioni

Subunit structurei

Interacts with DBNL/ABP1 and CTTN. May interact with CCPG1 (By similarity). Binds CDC42.By similarity

Protein-protein interaction databases

BioGridi108536. 4 interactions.
MINTiMINT-2805047.
STRINGi9606.ENSP00000364277.

Structurei

3D structure databases

ProteinModelPortaliP98174.
SMRiP98174. Positions 316-786, 831-920.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini373 – 561189DHPROSITE-ProRule annotationAdd
BLAST
Domaini590 – 689100PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini821 – 921101PH 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi171 – 18717SH3-bindingSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 330324Pro-richAdd
BLAST

Domaini

The DH domain is involved in interaction with CCPG1.By similarity

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri730 – 79061FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG295069.
GeneTreeiENSGT00750000117280.
HOGENOMiHOG000220866.
HOVERGENiHBG007506.
InParanoidiP98174.
KOiK05720.
OMAiLQMPRMP.
OrthoDBiEOG7C2R0M.
PhylomeDBiP98174.
TreeFamiTF316247.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF00169. PH. 2 hits.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P98174-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHGHRAPGGA GPSEPEHPAT NPPGAAPPAC ADSDPGASEP GLLARRGSGS
60 70 80 90 100
ALGGPLDPQF VGPSDTSLGA APGHRVLPCG PSPQHHRALR FSYHLEGSQP
110 120 130 140 150
RPGLHQGNRI LVKSLSLDPG QSLEPHPEGP QRLRSDPGPP TETPSQRPSP
160 170 180 190 200
LKRAPGPKPQ VPPKPSYLQM PRMPPPLEPI PPPPSRPLPA DPRVAKGLAP
210 220 230 240 250
RAEASPSSAA VSSLIEKFER EPVIVASDRP VPGPSPGPPE PVMLPQPTSQ
260 270 280 290 300
PPVPQLPEGE ASRCLFLLAP GPRDGEKVPN RDSGIDSISS PSNSEETCFV
310 320 330 340 350
SDDGPPSHSL CPGPPALASV PVALADPHRP GSQEVDSDLE EEDDEEEEEE
360 370 380 390 400
KDREIPVPLM ERQESVELTV QQKVFHIANE LLQTEKAYVS RLHLLDQVFC
410 420 430 440 450
ARLLEEARNR SSFPADVVHG IFSNICSIYC FHQQFLLPEL EKRMEEWDRY
460 470 480 490 500
PRIGDILQKL APFLKMYGEY VKNFDRAVEL VNTWTERSTQ FKVIIHEVQK
510 520 530 540 550
EEACGNLTLQ HHMLEPVQRI PRYELLLKDY LLKLPHGSPD SKDAQKSLEL
560 570 580 590 600
IATAAEHSNA AIRKMERMHK LLKVYELLGG EEDIVSPTKE LIKEGHILKL
610 620 630 640 650
SAKNGTTQDR YLILFNDRLL YCVPRLRLLG QKFSVRARID VDGMELKESS
660 670 680 690 700
NLNLPRTFLV SGKQRSLELQ ARTEEEKKDW VQAINSTLLK HEQTLETFKL
710 720 730 740 750
LNSTNREDED TPPNSPNVDL GKRAPTPIRE KEVTMCMRCQ EPFNSITKRR
760 770 780 790 800
HHCKACGHVV CGKCSEFRAR LVYDNNRSNR VCTDCYVALH GVPGSSPACS
810 820 830 840 850
QHTPQRRRSI LEKQASVAAE NSVICSFLHY MEKGGKGWHK AWFVVPENEP
860 870 880 890 900
LVLYIYGAPQ DVKAQRSLPL IGFEVGPPEA GERPDRRHVF KITQSHLSWY
910 920 930 940 950
FSPETEELQR RWMAVLGRAG RGDTFCPGPT LSEDREMEEA PVAALGATAE
960
PPESPQTRDK T
Length:961
Mass (Da):106,561
Last modified:February 1, 2003 - v2
Checksum:i30963F7B9931E45C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 2314AGPSE…ATNPP → RRAFGARTPGHEPA (PubMed:7954831).CuratedAdd
BLAST
Sequence conflicti195 – 1951A → G in AAA57004 (PubMed:7954831).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti205 – 2051S → I in AAS. 1 Publication
VAR_019268
Natural varianti312 – 3121P → L in non-syndromal X-linked mental retardation. 1 Publication
Corresponds to variant rs28935498 [ dbSNP | Ensembl ].
VAR_019269
Natural varianti380 – 3801E → A in AAS. 1 Publication
VAR_019270
Natural varianti443 – 4431R → H in AAS. 1 Publication
VAR_019271
Natural varianti522 – 5221R → H in AAS. 1 Publication
VAR_015236
Natural varianti610 – 6101R → Q in AAS. 1 Publication
Corresponds to variant rs28935497 [ dbSNP | Ensembl ].
VAR_015237

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11690 mRNA. Translation: AAA57004.1.
Z85987 Genomic DNA. Translation: CAI42222.1.
CH471154 Genomic DNA. Translation: EAW93179.1.
BC034530 mRNA. Translation: AAH34530.1.
CCDSiCCDS14359.1.
PIRiA55380.
RefSeqiNP_004454.2. NM_004463.2.
UniGeneiHs.709201.

Genome annotation databases

EnsembliENST00000375135; ENSP00000364277; ENSG00000102302.
GeneIDi2245.
KEGGihsa:2245.
UCSCiuc004dtg.3. human.

Polymorphism and mutation databases

BioMutaiFGD1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11690 mRNA. Translation: AAA57004.1.
Z85987 Genomic DNA. Translation: CAI42222.1.
CH471154 Genomic DNA. Translation: EAW93179.1.
BC034530 mRNA. Translation: AAH34530.1.
CCDSiCCDS14359.1.
PIRiA55380.
RefSeqiNP_004454.2. NM_004463.2.
UniGeneiHs.709201.

3D structure databases

ProteinModelPortaliP98174.
SMRiP98174. Positions 316-786, 831-920.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108536. 4 interactions.
MINTiMINT-2805047.
STRINGi9606.ENSP00000364277.

Chemistry

BindingDBiP98174.
ChEMBLiCHEMBL2862.

PTM databases

PhosphoSiteiP98174.

Polymorphism and mutation databases

BioMutaiFGD1.
DMDMi28202247.

Proteomic databases

MaxQBiP98174.
PaxDbiP98174.
PRIDEiP98174.

Protocols and materials databases

DNASUi2245.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375135; ENSP00000364277; ENSG00000102302.
GeneIDi2245.
KEGGihsa:2245.
UCSCiuc004dtg.3. human.

Organism-specific databases

CTDi2245.
GeneCardsiGC0XM054488.
HGNCiHGNC:3663. FGD1.
HPAiHPA000911.
MIMi300546. gene.
305400. phenotype.
neXtProtiNX_P98174.
Orphaneti915. Aarskog-Scott syndrome.
PharmGKBiPA28102.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG295069.
GeneTreeiENSGT00750000117280.
HOGENOMiHOG000220866.
HOVERGENiHBG007506.
InParanoidiP98174.
KOiK05720.
OMAiLQMPRMP.
OrthoDBiEOG7C2R0M.
PhylomeDBiP98174.
TreeFamiTF316247.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.

Miscellaneous databases

ChiTaRSiFGD1. human.
GeneWikiiFGD1.
GenomeRNAii2245.
NextBioi9083.
PROiP98174.
SOURCEiSearch...

Gene expression databases

BgeeiP98174.
CleanExiHS_FGD1.
ExpressionAtlasiP98174. baseline and differential.
GenevestigatoriP98174.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF00169. PH. 2 hits.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: a putative Rho/Rac guanine nucleotide exchange factor."
    Pasteris N.G., Cadle A., Logie L.J., Porteous M.E.M., Schwartz C.E., Stevenson R.E., Glover T.W., Wilroy R.S., Gorski J.L.
    Cell 79:669-678(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Craniofacial.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factor."
    Zheng Y., Fischer D.J., Santos M.F., Tigyi G., Pasteris N.G., Gorski J.L., Xu Y.
    J. Biol. Chem. 271:33169-33172(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-205; THR-711 AND SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Two novel mutations confirm FGD1 is responsible for the Aarskog syndrome."
    Schwartz C.E., Gillessen-Kaesbach G., May M., Cappa M., Gorski J.L., Steindl K., Neri G.
    Eur. J. Hum. Genet. 8:869-874(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AAS HIS-522.
  9. "A mutation in the pleckstrin homology (PH) domain of the FGD1 gene in an Italian family with faciogenital dysplasia (Aarskog-Scott syndrome)."
    Orrico A., Galli L., Falciani M., Bracci M., Cavaliere M.L., Rinaldi M.M., Musacchio A., Sorrentino V.
    FEBS Lett. 478:216-220(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AAS GLN-610.
  10. "Non-syndromic X-linked mental retardation associated with a missense mutation (P312L) in the FGD1 gene."
    Lebel R.R., May M., Pouls S., Lubs H.A., Stevenson R.E., Schwartz C.E.
    Clin. Genet. 61:139-145(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NONSYNDROMAL X-LINKED MENTAL RETARDATION LEU-312.
  11. "Phenotypic and molecular characterisation of the Aarskog-Scott syndrome: a survey of the clinical variability in light of FGD1 mutation analysis in 46 patients."
    Orrico A., Galli L., Cavaliere M.L., Garavelli L., Fryns J.-P., Crushell E., Rinaldi M.M., Medeira A., Sorrentino V.
    Eur. J. Hum. Genet. 12:16-23(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AAS ILE-205; ALA-380 AND HIS-443.

Entry informationi

Entry nameiFGD1_HUMAN
AccessioniPrimary (citable) accession number: P98174
Secondary accession number(s): Q5H999, Q8N4D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 1, 2003
Last modified: April 29, 2015
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.